EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
    2.8.1.7 | L-cysteine |
unlike other cysteine desulfurases the L-cysteine C-S-lyase from Synechocystis does not have a conserved cysteine residue at the active site |
Synechocystis sp. |
L-alanine + sulfide |
- |
? |
| 2.8.1.7 | L-cysteine |
unlike other cysteine desulfurases the L-cysteine C-S-lyase from Synechocystis does not have a conserved cysteine residue at the active site |
Synechocystis sp. PCC6714 |
L-alanine + sulfide |
- |
? |
| 2.8.1.7 | L-cysteine |
- |
Nostoc sp. PCC 7120 = FACHB-418 |
L-alanine + H2S |
- |
? |
| 2.8.1.7 | L-cysteine |
- |
Acidithiobacillus ferrooxidans |
L-alanine + H2S |
or formation of elemental sulfur, depending of presence of a reducing agent in the reaction mixture |
? |
| 2.8.1.7 | L-cysteine |
DndA is able to directly activate apo-Fe DndC for its reconstitution as a fully functional [4Fe-4S] cluster protein (DndC) with unambiguously demonstrated ATP pyrophosphatase activity |
Streptomyces lividans |
L-alanine + sulfur |
- |
? |
| 2.8.1.7 | L-cysteine + ? |
in the presence of cysteine, IscSs ability to bind iron improves significantly |
Escherichia coli |
? |
- |
? |
| 2.8.1.7 | L-cysteine + ? |
catalyzes the elimination of S from L-cysteine to yield L-alanine and elemental sulfur or H2S, depending on whether or not a reducing agent is added to the reaction mixture, provides sulfur for the assembly of ironsulfur cluster |
Acidithiobacillus ferrooxidans |
L-alanine + ? |
- |
? |
| 2.8.1.7 | L-cysteine + acceptor |
overall reaction, the enzyme shows a selenocysteine lyase activity approximately 280fold higher than its cysteine desulfurase activity. The desulfuration mechanism proposed for this enzyme seems to involve three different stages. At the beginning of the reaction, L-cysteine is quickly bound by the cofactor pyridoxal 5'-phosphate, shifting the UV-VIS spectrum of the enzyme. In this aldimine state, the L-cysteine sulfur atom is attacked by Cys384, resulting in persulfide formation. To regenerate the enzyme, this persulfide state must be resolved by transferring the sulphide to inorganic or organic acceptor molecules (accessory proteins, DTT or to other L-cysteine molecules) |
Haloferax volcanii |
L-alanine + sulfide + ? |
- |
? |
| 2.8.1.7 | L-cysteine + acceptor |
overall reaction, the enzyme shows a selenocysteine lyase activity approximately 280fold higher than its cysteine desulfurase activity. The desulfuration mechanism proposed for this enzyme seems to involve three different stages. At the beginning of the reaction, L-cysteine is quickly bound by the cofactor pyridoxal 5'-phosphate, shifting the UV-VIS spectrum of the enzyme. In this aldimine state, the L-cysteine sulfur atom is attacked by Cys384, resulting in persulfide formation. To regenerate the enzyme, this persulfide state must be resolved by transferring the sulphide to inorganic or organic acceptor molecules (accessory proteins, DTT or to other L-cysteine molecules) |
Haloferax volcanii DSM 3757 |
L-alanine + sulfide + ? |
- |
? |
| 2.8.1.7 | L-cysteine + acceptor |
- |
Saccharomyces cerevisiae |
L-alanine + S-sulfanyl-acceptor |
- |
? |
